ID   ASPA_ECOL6              Reviewed;         478 AA.
AC   P0AC39; P04422; P78140;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Aspartate ammonia-lyase;
DE            Short=Aspartase;
DE            EC=4.3.1.1;
GN   Name=aspA; OrderedLocusNames=c5222;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83644.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000069437.1; NC_004431.1.
DR   AlphaFoldDB; P0AC39; -.
DR   SMR; P0AC39; -.
DR   STRING; 199310.c5222; -.
DR   EnsemblBacteria; AAN83644; AAN83644; c5222.
DR   GeneID; 66671949; -.
DR   KEGG; ecc:c5222; -.
DR   eggNOG; COG1027; Bacteria.
DR   HOGENOM; CLU_021594_4_0_6; -.
DR   OMA; EICENYV; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR004708; ApsA.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00839; aspA; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..478
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161340"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  52356 MW;  B6E8432DBF385DEA CRC64;
     MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNNK ISDIPEFVRG MVMVKKAAAM
     ANKELQTIPK SVANAIIAAC DEVLNNGKCM DQFPVDVYQG GAGTSVNMNT NEVLANIGLE
     LMGHQKGEYQ YLNPNDHVNK CQSTNDAYPT GFRIAVYSSL IKLVDAINQL REGFERKAVE
     FQDILKMGRT QLQDAVPMTL GQEFRAFSIL LKEEVKNIQR TAELLLEVNL GATAIGTGLN
     TPKEYSPLAV KKLAEVTGFP CVPAEDLIEA TSDCGAYVMV HGALKRLAVK MSKICNDLRL
     LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTTV TMAAEAGQLQ
     LNVMEPVIGQ AMFESVHILT NACYNLLEKC INGITANKEV CEGYVYNSIG IVTYLNPFIG
     HHNGDIVGKI CAETGKSVRE VVLERGLLTE AELDDIFSVQ NLMHPAYKAK RYTDESEQ